Physicochemical and structural properties of lunasin revealed by spectroscopic, chromatographic and molecular dynamics approaches

Lunasin as a Promising Plant-Derived Peptide for Cancer Therapy

“…As a result, lunasin has a theoretical pI of approximately 4.43 ( , accessed on 8 June 2021). Its sequence also contains many hydrophilic and charged residues that make the peptide intrinsically disordered [ 24 ].…”

“…Structural changes and aberrant disulfide bond formation may occur during the manufacturing of therapeutic proteins, presenting a challenge [ 35 ]. The primary structure of lunasin contains two cysteine (C) residues (at positions 10 and 22 of the polypeptide chain) that can form intramolecular disulfide bond as has been reported in synthetic and recombinant forms [ 24 , 36 ]. Cysteines on the lunasin sequence are either reduced or oxidized, depending on environmental conditions [ 36 ].…”

“…Cysteines on the lunasin sequence are either reduced or oxidized, depending on environmental conditions [ 36 ]. In aqueous solutions, lunasin cysteines tend to be oxidized, eventually forming intramolecular bonds [ 24 , 36 ]. The biological implications of this intramolecular bond formation remain unclear but may be related to lunasin’s anti-inflammatory and antioxidant activities [ 36 ].…”

“…Studies performed with recombinant and synthetic lunasin have indicated a mostly unordered structure with transient α-helices [ 24 , 36 ]. Transient helices can be favored and stabilized depending on the conditions or on specific binding to certain molecular partners.…”

“…Transient helices can be favored and stabilized depending on the conditions or on specific binding to certain molecular partners. Protonation of aspartic acid (D) residues did not reveal significant alterations in the secondary structure [ 24 , 36 ]. Available data suggest that lunasin is an intrinsically disordered peptide in a pre-molten globule-like state [ 24 ].…”